5uhu
From Proteopedia
(Difference between revisions)
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| - | '''Unreleased structure''' | ||
| - | + | ==Solution conformation of cytochrome P450 MycG with mycinamicin IV bound== | |
| + | <StructureSection load='5uhu' size='340' side='right' caption='[[5uhu]], [[NMR_Ensembles_of_Models | 1 NMR models]]' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[5uhu]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5UHU OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5UHU FirstGlance]. <br> | ||
| + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=MIV:MYCINAMICIN+IV'>MIV</scene></td></tr> | ||
| + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2y98|2y98]]</td></tr> | ||
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5uhu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5uhu OCA], [http://pdbe.org/5uhu PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5uhu RCSB], [http://www.ebi.ac.uk/pdbsum/5uhu PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5uhu ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [[http://www.uniprot.org/uniprot/MYCG_MICGR MYCG_MICGR]] Involved in the biosynthesis of mycinamicin, a 16-membered macrolide antibiotic. Catalyzes consecutive hydroxylation (at C14) and epoxidation (at C12-C13) reactions with mycinamicin IV as initial substrate, leading to mycinamicin II. These reactions require prior dimethylation of 6-deoxyallose to mycinose for effective conversion by the dual function MycG enzyme.<ref>PMID:18804032</ref> <ref>PMID:22547618</ref> <ref>PMID:7808395</ref> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | MycG is a P450 monooxygenase that catalyzes the sequential hydroxylation and epoxidation of mycinamicin IV (M-IV), the last two steps in the biosynthesis of mycinamicin II, a macrolide antibiotic isolated from Micromonospora griseorubida. The crystal structure of MycG with M-IV bound was previously determined but showed the bound substrate in an orientation that did not rationalize the observed regiochemistry of M-IV hydroxylation. Nuclear magnetic resonance paramagnetic relaxation enhancements provided evidence of an orientation of M-IV in the MycG active site more compatible with the observed chemistry, but substrate-induced changes in the enzyme structure were not characterized. We now describe the use of amide 1H-15N residual dipolar couplings as experimental restraints in solvated "soft annealing" molecular dynamics simulations to generate solution structural ensembles of M-IV-bound MycG. Chemical shift perturbations, hydrogen-deuterium exchange, and 15N relaxation behavior provide insight into the dynamic and electronic perturbations in the MycG structure in response to M-IV binding. The solution and crystallographic structures are compared, and the possibility that the crystallographic orientation of bound M-IV represents an inhibitory mode is discussed. | ||
| - | + | Solution Conformations and Dynamics of Substrate-Bound Cytochrome P450 MycG.,Tietz DR, Podust LM, Sherman DH, Pochapsky TC Biochemistry. 2017 May 30;56(21):2701-2714. doi: 10.1021/acs.biochem.7b00291., Epub 2017 May 16. PMID:28488849<ref>PMID:28488849</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | [[Category: Pochapsky, T | + | <div class="pdbe-citations 5uhu" style="background-color:#fffaf0;"></div> |
| - | [[Category: Tietz, D | + | == References == |
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Pochapsky, T C]] | ||
| + | [[Category: Tietz, D R]] | ||
| + | [[Category: Antibiotic biosynthesis]] | ||
| + | [[Category: Oxidoreductase]] | ||
Revision as of 11:12, 24 August 2017
Solution conformation of cytochrome P450 MycG with mycinamicin IV bound
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